An spin-labelling methodology provides structural information on cytoplasmic proteins in bacteria

EPR in-cell spin-labeling was applied to CueR in E. coli . The methodology employed a Cu( ii )-NTA complexed with dHis. High resolved in-cell distance distributions were obtained revealing minor differences between in vitro and in-cell data. This methodology allows study of structural changes of any protein in-cell, independent of size or cellular system. EPR in-cell spin-labeling was applied to CueR in E. coli .